Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Pohl, B.; Schmidt, W.
    Comparative studies of purified and reconstituted monoamine oxidase from bovine liver mitochondria (1983), Biochim. Biophys. Acta, 731, 338-345.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.3.4 deoxycholate
-
 Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.4 additional information
-
 additional information effect of phospholipids on Km Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
1.4.3.4 deoxycholate
-
 Bos taurus
1.4.3.4 Triton X-100 disintegrates the lipid-enzyme cluster to the smallest active units Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.4 Bos taurus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.4.3.4 additional information the lipid enviroment appears to be an indispensable prerequisite for proper enzyme activity Bos taurus

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.3.4
-
 Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.4.3.4 liver
-
 Bos taurus
-

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.4.3.4 additional information
-
 temperature-dependencies of enzyme activity of purified and lipid-treated enzyme Bos taurus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.3.4 8
-
 purified enzyme Bos taurus
1.4.3.4 8 10 phosphatidylcholine-treated enzyme Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.4 flavin flavoprotein Bos taurus